Literature summary for 1.3.2.3 extracted from

Rodriguez-Ruiz, M.; Mateos, R.M.; Codesido, V.; Corpas, F.J.; Palma, J.M.
Characterization of the galactono-1,4-lactone dehydrogenase from pepper fruits and its modulation in the ascorbate biosynthesis. Role of nitric oxide (2017), Redox Biol., 12, 171-181 .

Search for more literature for 1.3.2.3

Cloned(Commentary)

Cloned (Comment)	Organism
gene GLDH1, DNA and amino acid sequence determination and analysis, quantitative real-time PCR enzyme expression analysis	Capsicum annuum

Inhibitors

Inhibitors	Comment	Organism	Structure
glutathione	the enzyme activity is inhibited by 60% by reduced glutathione (GSH)	Capsicum annuum
additional information	incubation of pepper crude extracts with increasing concentrations of SIN-1, a peroxynitrite donor, does not modify GalLDH activity significantly. Similarly, S-nitrosoglutathione, GSNO, an NO donor, does not affect the enzyme activity either	Capsicum annuum

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	GalLDH from pepper fruits is attached to the mitochondrial membrane through, at least, a very short transmembrane domain of 20 amino acids, with the rest of the protein structure being peripheral	Capsicum annuum	5739	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-galactono-1,4-lactone + 4 ferricytochrome c	Capsicum annuum	overall reaction	L-dehydroascorbate + 4 ferrocytochrome c + 4 H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Capsicum annuum	Q6QD76	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
flower	very high enzyme expression but very low enzyme activity	Capsicum annuum	-
fruit	green and red fruits	Capsicum annuum	-
leaf	high enzyme expression but low enzyme activity	Capsicum annuum	-
additional information	GalLDH activity occurs in fruits, leaves, flowers, and stems, with higher values obtained in fruits and stem. No significant differences are detected between green and red fruits	Capsicum annuum	-
stem	-	Capsicum annuum	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-galactono-1,4-lactone + 4 ferricytochrome c	overall reaction	Capsicum annuum	L-dehydroascorbate + 4 ferrocytochrome c + 4 H+	-	?

Subunits

Subunits	Comment	Organism
?	x * 62200, about, sequence calculation	Capsicum annuum

Synonyms

Synonyms	Comment	Organism
galactono-1,4-lactone dehydrogenase	-	Capsicum annuum
GalLDH	-	Capsicum annuum
GLDH1	-	Capsicum annuum
L-galactono-1,4-lactone dehydrogenase	-	Capsicum annuum

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Capsicum annuum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.4	-	assay at	Capsicum annuum

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome c	-	Capsicum annuum
FAD	-	Capsicum annuum

pI Value

Organism	Comment	pI Value Maximum	pI Value
Capsicum annuum	sequence calculation	-	6.4

Expression

Organism	Comment	Expression
Capsicum annuum	expression of the GalLDH gene is drastically induced about 13fold after the incubation with nitric monooxide	up

General Information

General Information	Comment	Organism
physiological function	GalLDH is a key modulation point of the physiology of pepper plants. GalLDH might have a pivotal role which allows the interaction with several neighboring respiratory oxidases. GalLDH is an unstable protein, and this contributes to maintain and even increase the ascorbate levels, it has also an important role during development and fruit ripening. Respiration can control ascorbate synthesis in plants and for its optimum biosynthesis is necessary an electron flux through the complex I of the mitochondrial electron transport chain. In vitro experiments on GalLDH activity in the presence of GSH show, the ascorbate levels in pepper fruits also depend on the redox chemical surrounding of the GalLDH, since this enzyme activity is inhibited by GSH	Capsicum annuum

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Release 2023.1 (January 2023)